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Water retention capabilities of collagen, gelatin and peptide as studied by IR/QCM/RH system.
Spectrochim Acta A Mol Biomol Spectrosc. 2020 Jun 19; 241:118619.SA

Abstract

In this study, water retention properties of triple helix collagen, gelatin (separated single chains) and peptide (broken peptide fragments) were studied by using IR micro-spectroscopy equipped with a relative humidity (RH) control system and quartz crystal microbalance (QCM). Adsorbed water ratios (wt%) are found to be in the order of collagen, gelatin and peptide (at about RH = 60%, 22 wt% for collagen, 14 wt% for gelatin and 9 wt% for peptide). Free water molecules with longer H bonds are the major adsorbed water species for collagen, gelatin and peptide. IR band shifts and changes in normalized band areas of functional groups are generally larger for collagen than gelatin and peptide, indicating larger interactions of water molecules with functional groups such as aliphatic CH2, CH3, amides, COO- and C-O for collagen. Relations between normalized band areas show that water molecules are interacting with aliphatic CH species and C-O bonds of collagen. Since the fibril structures of collagen triple helices are reported to be cross-linked by sugars, water molecules can be attracted to polar C-O bonds of sugars linking collagen triple helices in fibrils and they are interacting with adjacent aliphatic CH side chains on the surface of fibrils.

Authors+Show Affiliations

Department of Earth and Space Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan; Taki Chemical Co., Ltd., 346 Miyanishi, Harima-cho, Kako-gun, Hyogo 675-0145, Japan.Department of Earth and Space Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan; Faculty of Environmental and Urban Engineering, Kansai University, Yamate-cho 3-3-35, Suita-shi, Osaka 564-8680, Japan; Research Institute for Natural Environment, Science and Technology (RINEST), Tarumi-cho 3-6-32 Maison Esaka 1F, Suita-shi, Osaka 564-0062, Japan. Electronic address: SatoruNakashima.ed@gmail.com.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32622049

Citation

Kudo, Sachie, and Satoru Nakashima. "Water Retention Capabilities of Collagen, Gelatin and Peptide as Studied By IR/QCM/RH System." Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, vol. 241, 2020, p. 118619.
Kudo S, Nakashima S. Water retention capabilities of collagen, gelatin and peptide as studied by IR/QCM/RH system. Spectrochim Acta A Mol Biomol Spectrosc. 2020;241:118619.
Kudo, S., & Nakashima, S. (2020). Water retention capabilities of collagen, gelatin and peptide as studied by IR/QCM/RH system. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 241, 118619. https://doi.org/10.1016/j.saa.2020.118619
Kudo S, Nakashima S. Water Retention Capabilities of Collagen, Gelatin and Peptide as Studied By IR/QCM/RH System. Spectrochim Acta A Mol Biomol Spectrosc. 2020 Jun 19;241:118619. PubMed PMID: 32622049.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Water retention capabilities of collagen, gelatin and peptide as studied by IR/QCM/RH system. AU - Kudo,Sachie, AU - Nakashima,Satoru, Y1 - 2020/06/19/ PY - 2020/01/15/received PY - 2020/06/10/revised PY - 2020/06/13/accepted PY - 2020/7/6/pubmed PY - 2020/7/6/medline PY - 2020/7/5/entrez KW - Collagen KW - Gelatin KW - Hydrogen bonding KW - Infrared spectroscopy KW - Peptide KW - Water molecules SP - 118619 EP - 118619 JF - Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy JO - Spectrochim Acta A Mol Biomol Spectrosc VL - 241 N2 - In this study, water retention properties of triple helix collagen, gelatin (separated single chains) and peptide (broken peptide fragments) were studied by using IR micro-spectroscopy equipped with a relative humidity (RH) control system and quartz crystal microbalance (QCM). Adsorbed water ratios (wt%) are found to be in the order of collagen, gelatin and peptide (at about RH = 60%, 22 wt% for collagen, 14 wt% for gelatin and 9 wt% for peptide). Free water molecules with longer H bonds are the major adsorbed water species for collagen, gelatin and peptide. IR band shifts and changes in normalized band areas of functional groups are generally larger for collagen than gelatin and peptide, indicating larger interactions of water molecules with functional groups such as aliphatic CH2, CH3, amides, COO- and C-O for collagen. Relations between normalized band areas show that water molecules are interacting with aliphatic CH species and C-O bonds of collagen. Since the fibril structures of collagen triple helices are reported to be cross-linked by sugars, water molecules can be attracted to polar C-O bonds of sugars linking collagen triple helices in fibrils and they are interacting with adjacent aliphatic CH side chains on the surface of fibrils. SN - 1873-3557 UR - https://www.unboundmedicine.com/medline/citation/32622049/Water_retention_capabilities_of_collagen,_gelatin_and_peptide_as_studied_by_IR/QCM/RH_system L2 - https://linkinghub.elsevier.com/retrieve/pii/S1386-1425(20)30598-9 DB - PRIME DP - Unbound Medicine ER -
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